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- EMDB-55800: Integrin AlphaIIbBeta3 bound to Fab of the anti-HPA-1a antibody 26.4 -

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Basic information

Entry
Database: EMDB / ID: EMD-55800
TitleIntegrin AlphaIIbBeta3 bound to Fab of the anti-HPA-1a antibody 26.4
Map dataPrimary map
Sample
  • Complex: Complex of integrin aIIbb3 ectodomains bound to the Fab 26.4
    • Protein or peptide: Integrin alpha-IIb
    • Protein or peptide: Integrin beta-3
    • Protein or peptide: Antibody 26.4 Fab heavy chain
    • Protein or peptide: Antibody 26.4 Fab light chain
  • Ligand: CALCIUM ION
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: MAGNESIUM ION
  • Ligand: water
KeywordsHuman Platelet Antigen / FNAIT / alloantibody / cryo-EM / CELL ADHESION
Function / homology
Function and homology information


regulation of serotonin uptake / positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway / tube development / alpha9-beta1 integrin-ADAM8 complex / regulation of trophoblast cell migration / integrin alphaIIb-beta3 complex / regulation of postsynaptic neurotransmitter receptor diffusion trapping / maintenance of postsynaptic specialization structure / alphav-beta3 integrin-vitronectin complex / regulation of extracellular matrix organization ...regulation of serotonin uptake / positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway / tube development / alpha9-beta1 integrin-ADAM8 complex / regulation of trophoblast cell migration / integrin alphaIIb-beta3 complex / regulation of postsynaptic neurotransmitter receptor diffusion trapping / maintenance of postsynaptic specialization structure / alphav-beta3 integrin-vitronectin complex / regulation of extracellular matrix organization / platelet alpha granule membrane / positive regulation of glomerular mesangial cell proliferation / integrin alphav-beta3 complex / negative regulation of lipoprotein metabolic process / alphav-beta3 integrin-PKCalpha complex / fibrinogen binding / alphav-beta3 integrin-HMGB1 complex / negative regulation of lipid transport / vascular endothelial growth factor receptor 2 binding / positive regulation of vascular endothelial growth factor signaling pathway / Elastic fibre formation / cell-substrate junction assembly / alphav-beta3 integrin-IGF-1-IGF1R complex / positive regulation of bone resorption / platelet-derived growth factor receptor binding / mesodermal cell differentiation / glycinergic synapse / filopodium membrane / extracellular matrix binding / regulation of release of sequestered calcium ion into cytosol / positive regulation of cell adhesion mediated by integrin / apolipoprotein A-I-mediated signaling pathway / positive regulation of vascular endothelial growth factor receptor signaling pathway / regulation of bone resorption / negative regulation of low-density lipoprotein particle clearance / angiogenesis involved in wound healing / wound healing, spreading of epidermal cells / positive regulation of leukocyte migration / apoptotic cell clearance / positive regulation of fibroblast migration / integrin complex / cell adhesion mediated by integrin / smooth muscle cell migration / Molecules associated with elastic fibres / heterotypic cell-cell adhesion / positive regulation of smooth muscle cell migration / negative chemotaxis / Mechanical load activates signaling by PIEZO1 and integrins in osteocytes / Syndecan interactions / positive regulation of cell-matrix adhesion / p130Cas linkage to MAPK signaling for integrins / regulation of postsynaptic neurotransmitter receptor internalization / cellular response to insulin-like growth factor stimulus / positive regulation of osteoblast proliferation / protein disulfide isomerase activity / microvillus membrane / cell-substrate adhesion / platelet-derived growth factor receptor signaling pathway / PECAM1 interactions / GRB2:SOS provides linkage to MAPK signaling for Integrins / TGF-beta receptor signaling activates SMADs / lamellipodium membrane / fibronectin binding / negative regulation of macrophage derived foam cell differentiation / negative regulation of lipid storage / blood coagulation, fibrin clot formation / ECM proteoglycans / Integrin cell surface interactions / negative regulation of endothelial cell apoptotic process / positive regulation of T cell migration / coreceptor activity / cellular response to platelet-derived growth factor stimulus / Integrin signaling / positive regulation of endothelial cell proliferation / positive regulation of substrate adhesion-dependent cell spreading / substrate adhesion-dependent cell spreading / embryo implantation / cell adhesion molecule binding / positive regulation of endothelial cell migration / positive regulation of smooth muscle cell proliferation / Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells / cell-matrix adhesion / protein kinase C binding / response to activity / Signal transduction by L1 / integrin-mediated signaling pathway / regulation of actin cytoskeleton organization / wound healing / cellular response to mechanical stimulus / cell-cell adhesion / Signaling by high-kinase activity BRAF mutants / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / MAP2K and MAPK activation / platelet activation / VEGFA-VEGFR2 Pathway / platelet aggregation / integrin binding / cellular response to xenobiotic stimulus / positive regulation of fibroblast proliferation / ruffle membrane
Similarity search - Function
Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / : / Integrin alpha Ig-like domain 3 / Integrin beta subunit, cytoplasmic domain / Integrin beta tail domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / : / Integrin EGF domain ...Integrin beta, epidermal growth factor-like domain 1 / Integrin beta epidermal growth factor like domain 1 / : / Integrin alpha Ig-like domain 3 / Integrin beta subunit, cytoplasmic domain / Integrin beta tail domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / : / Integrin EGF domain / EGF-like domain, extracellular / EGF-like domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily / Integrin_B_tail / Integrin alpha cytoplasmic region / : / Integrins beta chain EGF (I-EGF) domain profile. / Integrin beta subunit, VWA domain / Integrin beta subunit / Integrin beta N-terminal / Integrin beta chain VWA domain / Integrin plexin domain / Integrins beta chain EGF (I-EGF) domain signature. / Integrin beta subunits (N-terminal portion of extracellular region) / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / Integrin alpha chain, C-terminal cytoplasmic region, conserved site / Integrins alpha chain signature. / Integrin alpha chain / Integrin alpha beta-propellor / : / Integrin alpha Ig-like domain 2 / FG-GAP repeat profile. / Integrin alpha (beta-propellor repeats). / FG-GAP repeat / FG-GAP repeat / Integrin domain superfamily / Integrin alpha, N-terminal / PSI domain / domain found in Plexins, Semaphorins and Integrins / von Willebrand factor A-like domain superfamily / EGF-like domain signature 1. / EGF-like domain signature 2.
Similarity search - Domain/homology
Integrin beta-3 / Integrin alpha-IIb
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.64 Å
Authorsde Pereda JM / Stam W / Gragera M / van der Meer F / Chichon FJ / Zarkadas E / van der Schoot E / Vidarsson G / Takagi J / Margadant C
Funding support Netherlands, Spain, European Union, 6 items
OrganizationGrant numberCountry
Other private2019 Netherlands
Other private2336 Netherlands
Agencia Estatal de Investigacion (AEI)PID2022-136322NB-I00 Spain
Other government34459European Union
Other government37638European Union
Other government68606European Union
CitationJournal: To Be Published
Title: High-resolution cryo-EM structure of integrin aIIbb3 in complex with a disease-causing maternal HPA-1a antibody that blocks integrin activation
Authors: de Pereda JM / Stam W / Gragera M / van der Meer F / Chichon FJ / Zarkadas E / van der Schoot E / Vidarsson G / Takagi J / Margadant C
History
DepositionNov 22, 2025-
Header (metadata) releaseJun 10, 2026-
Map releaseJun 10, 2026-
UpdateJun 10, 2026-
Current statusJun 10, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_55800.png

Downloads & links

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Map

FileDownload / File: emd_55800.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPrimary map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.03 Å/pix.
x 300 pix.
= 309.52 Å		1.03 Å/pix.
x 300 pix.
= 309.52 Å		1.03 Å/pix.
x 300 pix.
= 309.52 Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.03173 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.16
Minimum - Maximum-0.7979947 - 1.7228419
Average (Standard dev.)0.0008339759 (±0.03521898)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 309.52 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_55800_msk_1.map
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Additional map: Sharpened map with deepEMhancer from the refined (main)...

Fileemd_55800_additional_1.map
AnnotationSharpened map with deepEMhancer from the refined (main) map; used for model refinement (manual rebuilding in Coot)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

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Additional map: Focused refinement map; used for model refinement (manual...

Fileemd_55800_additional_2.map
AnnotationFocused refinement map; used for model refinement (manual rebuilding in Coot).
Projections & Slices
AxesZYX

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Histogram

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Additional map: Half map B of the focused refinement map

Fileemd_55800_additional_3.map
AnnotationHalf map B of the focused refinement map
Projections & Slices
AxesZYX

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Histogram

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Additional map: Half map A of the focused refinement map

Fileemd_55800_additional_4.map
AnnotationHalf map A of the focused refinement map
Projections & Slices
AxesZYX

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Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focused refinement map sharpened with deepEMhancer; used for...

Fileemd_55800_additional_5.map
AnnotationFocused refinement map sharpened with deepEMhancer; used for model refinement (manual rebuilding in Coot).
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map B of the primary map

Fileemd_55800_half_map_1.map
AnnotationHalf map B of the primary map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map A of the primary map

Fileemd_55800_half_map_2.map
AnnotationHalf map A of the primary map
Projections & Slices
AxesZYX

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Histogram

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Sample components

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Entire : Complex of integrin aIIbb3 ectodomains bound to the Fab 26.4

EntireName: Complex of integrin aIIbb3 ectodomains bound to the Fab 26.4
Components
  • Complex: Complex of integrin aIIbb3 ectodomains bound to the Fab 26.4
    • Protein or peptide: Integrin alpha-IIb
    • Protein or peptide: Integrin beta-3
    • Protein or peptide: Antibody 26.4 Fab heavy chain
    • Protein or peptide: Antibody 26.4 Fab light chain
  • Ligand: CALCIUM ION
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: MAGNESIUM ION
  • Ligand: water

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Supramolecule #1: Complex of integrin aIIbb3 ectodomains bound to the Fab 26.4

SupramoleculeName: Complex of integrin aIIbb3 ectodomains bound to the Fab 26.4
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 240 KDa

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Macromolecule #1: Integrin alpha-IIb

MacromoleculeName: Integrin alpha-IIb / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 108.456141 KDa
Recombinant expressionOrganism: Cricetulus griseus (Chinese hamster)
SequenceString: LNLDPVQLTF YAGPNGSQFG FSLDFHKDSH GRVAIVVGAP RTLGPSQEET GGVFLCPWRA EGGQCPSLLF DLRDETRNVG SQTLQTFKA RQGLGASVVS WSDVIVACAP WQHWNVLEKT EEAEKTPVGS CFLAQPESGR RAEYSPCRGN TLSRIYVEND F SWDKRYCE ...String:
LNLDPVQLTF YAGPNGSQFG FSLDFHKDSH GRVAIVVGAP RTLGPSQEET GGVFLCPWRA EGGQCPSLLF DLRDETRNVG SQTLQTFKA RQGLGASVVS WSDVIVACAP WQHWNVLEKT EEAEKTPVGS CFLAQPESGR RAEYSPCRGN TLSRIYVEND F SWDKRYCE AGFSSVVTQA GELVLGAPGG YYFLGLLAQA PVADIFSSYR PGILLWHVSS QSLSFDSSNP EYFDGYWGYS VA VGEFDGD LNTTEYVVGA PTWSWTLGAV EILDSYYQRL HRLRGEQMAS YFGHSVAVTD VNGDGRHDLL VGAPLYMESR ADR KLAEVG RVYLFLQPRG PHALGAPSLL LTGTQLYGRF GSAIAPLGDL DRDGYNDIAV AAPYGGPSGR GQVLVFLGQS EGLR SRPSQ VLDSPFPTGS AFGFSLRGAV DIDDNGYPDL IVGAYGANQV AVYRAQPVVK ASVQLLVQDS LNPAVKSCVL PQTKT PVSC FNIQMCVGAT GHNIPQKLSL NAELQLDRQK PRQGRRVLLL GSQQAGTTLN LDLGGKHSPI CHTTMAFLRD EADFRD KLS PIVLSLNVSL PPTEAGMAPA VVLHGDTHVQ EQTRIVLDCG EDDVCVPQLQ LTASVTGSPL LVGADNVLEL QMDAANE GE GAYEAELAVH LPQGAHYMRA LSNVEGFERL ICNQKKENET RVVLCELGNP MKKNAQIGIA MLVSVGNLEE AGESVSFQ L QIRSKNSQNP NSKIVLLDVP VRAEAQVELR GNSFPASLVV AAEEGEREQN SLDSWGPKVE HTYELHNNGP GTVNGLHLS IHLPGQSQPS DLLYILDIQP QGGLQCFPQP PVNPLKVDWG LPIPSPSPIH PAHHKRDRRQ IFLPEPEQPS RLQDPVLVSC DSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL DQFVLQSHAW FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL E ERAAQCEK ELQALEKENA QLEWELQALE KELAQ

UniProtKB: Integrin alpha-IIb

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Macromolecule #2: Integrin beta-3

MacromoleculeName: Integrin beta-3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 81.402023 KDa
Recombinant expressionOrganism: Cricetulus griseus (Chinese hamster)
SequenceString: GPNICTTRGV SSCQQCLAVS PMCAWCSDEA LPLGSPRCDL KENLLKDNCA PESIEFPVSE ARVLEDRPLS DKGSGDSSQV TQVSPQRIA LRLRPDDSKN FSIQVRQVED YPVDIYYLMD LSYSMKDDLW SIQNLGTKLA TQMRKLTSNL RIGFGAFVDK P VSPYMYIS ...String:
GPNICTTRGV SSCQQCLAVS PMCAWCSDEA LPLGSPRCDL KENLLKDNCA PESIEFPVSE ARVLEDRPLS DKGSGDSSQV TQVSPQRIA LRLRPDDSKN FSIQVRQVED YPVDIYYLMD LSYSMKDDLW SIQNLGTKLA TQMRKLTSNL RIGFGAFVDK P VSPYMYIS PPEALENPCY DMKTTCLPMF GYKHVLTLTD QVTRFNEEVK KQSVSRNRDA PEGGFDAIMQ ATVCDEKIGW RN DASHLLV FTTDAKTHIA LDGRLAGIVQ PNDGQCHVGS DNHYSASTTM DYPSLGLMTE KLSQKNINLI FAVTENVVNL YQN YSELIP GTTVGVLSMD SSNVLQLIVD AYGKIRSKVE LEVRDLPEEL SLSFNATCLN NEVIPGLKSC MGLKIGDTVS FSIE AKVRG CPQEKEKSFT IKPVGFKDSL IVQVTFDCDC ACQAQAEPNS HRCNNGNGTF ECGVCRCGPG WLGSQCECSE EDYRP SQQD ECSPREGQPV CSQRGECLCG QCVCHSSDFG KITGKYCECD DFSCVRYKGE MCSGHGQCSC GDCLCDSDWT GYYCNC TTR TDTCMSSNGL LCSGRGKCEC GSCVCIQPGS YGDTCEKCPT CPDACTFKKE CVECKKFDRG ALHDENTCNR YCRDEIE SV KELKDTGKDA VNCTYKNEDD CVVRFQYYED SSGKSILYVV EEPECPKGPD GGLENLYFQG GKNAQCKKKL QALKKKNA Q LKWKLQALKK KLAQ

UniProtKB: Integrin beta-3

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Macromolecule #3: Antibody 26.4 Fab heavy chain

MacromoleculeName: Antibody 26.4 Fab heavy chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.033857 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: QVQLQQSGPG LVKPSQTLSL TCAISGDSVS SNSAAWNWIR QSPSRGLEWL GRTYFRSNWY NDYAASVKSR ITINQDTSKN QLSLQLNSV TPEDTAMYYC ARDGAWGGSS WWPGLPHHYY SGMDVWGQGT TVTVSSASTK GPSVFPLAPS SKSTSGGTAA L GCLVKDYF ...String:
QVQLQQSGPG LVKPSQTLSL TCAISGDSVS SNSAAWNWIR QSPSRGLEWL GRTYFRSNWY NDYAASVKSR ITINQDTSKN QLSLQLNSV TPEDTAMYYC ARDGAWGGSS WWPGLPHHYY SGMDVWGQGT TVTVSSASTK GPSVFPLAPS SKSTSGGTAA L GCLVKDYF PEPVTVSWNS GALTSGVHTF PAVLQSSGLY SLSSVVTVPS SSLGTQTYIC NVNHKPSNTK VDKRVEPKSC DK TH

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Macromolecule #4: Antibody 26.4 Fab light chain

MacromoleculeName: Antibody 26.4 Fab light chain / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.441012 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: EIVLTQSPAT LSLSPGERAT LSCRASQSVS SYLAWYQQKP GQAPRLLIYD ASKRATGIPA RFSGSGSGTD FSLTIRSLEP EDFAVYYCQ QRSDWQGLTF GGGTKVEIKT VAAPSVFIFP PSDEQLKSGT ASVVCLLNNF YPREAKVQWK VDNALQSGNS Q ESVTEQDS ...String:
EIVLTQSPAT LSLSPGERAT LSCRASQSVS SYLAWYQQKP GQAPRLLIYD ASKRATGIPA RFSGSGSGTD FSLTIRSLEP EDFAVYYCQ QRSDWQGLTF GGGTKVEIKT VAAPSVFIFP PSDEQLKSGT ASVVCLLNNF YPREAKVQWK VDNALQSGNS Q ESVTEQDS KDSTYSLSST LTLSKADYEK HKVYACEVTH QGLSSPVTKS FNRGECS

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Macromolecule #8: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 8 / Number of copies: 6 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #9: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 9 / Number of copies: 2 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Macromolecule #10: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 10 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #11: water

MacromoleculeName: water / type: ligand / ID: 11 / Number of copies: 9 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.13 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
50.0 mMTris-HClTris
150.0 mMNaClsodium chloride
1.0 mMCaCl2calcium chloride
1.0 mMMgCl2magnesium chloride

Details: 50 mM Tris-HCl, 150 mM NaCl, 1 mM CaCl2, 1 mM MgCl2, pH 7.5
GridModel: Quantifoil R0.6/1 / Material: COPPER/RHODIUM / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Details: 25 mA
VitrificationCryogen name: ETHANE / Chamber humidity: 94 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: blotting time 3 sec, blot force 3.

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: TFS Selectris X / Energy filter - Slit width: 10 eV
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Average exposure time: 2.93 sec. / Average electron dose: 41.57 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 165000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 6717934
CTF correctionSoftware - Name: cisTEM (ver. 5.0.2) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Details: cryoSPARC initial volume (Stochastic Gradient Descent-based)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 2.64 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.6.2) / Number images used: 84349
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.6.2)
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final 3D classificationNumber classes: 8 / Avg.num./class: 96438 / Software - Name: cryoSPARC (ver. 4.6.2)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

3fcs

chain_id: A, source_name: PDB, initial_model_type: experimental model

3fcs

chain_id: B, source_name: PDB, initial_model_type: experimental model
chain_id: H, source_name: AlphaFold, initial_model_type: in silico model
chain_id: L, source_name: AlphaFold, initial_model_type: in silico model
DetailsInitial rigid body fitting of individual domains was done using Coot
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9td2:
Integrin AlphaIIbBeta3 bound to Fab of the anti-HPA-1a antibody 26.4

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